ID A0A2K6U0R0_SAIBB Unreviewed; 433 AA.
AC A0A2K6U0R0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=N-lysine methyltransferase SMYD2 {ECO:0000256|ARBA:ARBA00024125};
DE EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182};
DE AltName: Full=Histone methyltransferase SMYD2 {ECO:0000256|ARBA:ARBA00032558};
DE AltName: Full=SET and MYND domain-containing protein 2 {ECO:0000256|ARBA:ARBA00033035};
GN Name=SMYD2 {ECO:0000313|Ensembl:ENSSBOP00000025503.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000025503.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000025503.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Protein-lysine N-methyltransferase that methylates both
CC histones and non-histone proteins, including p53/TP53 and RB1.
CC Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The
CC activity requires interaction with HSP90alpha. Shows even higher
CC methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of
CC p53/TP53, leading to decreased DNA-binding activity and subsequent
CC transcriptional regulation activity of p53/TP53. Monomethylates RB1 at
CC 'Lys-860'. {ECO:0000256|ARBA:ARBA00024002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000256|ARBA:ARBA00000944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000256|ARBA:ARBA00000587};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_003930406.1; XM_003930357.2.
DR AlphaFoldDB; A0A2K6U0R0; -.
DR STRING; 39432.ENSSBOP00000025503; -.
DR Ensembl; ENSSBOT00000042370.1; ENSSBOP00000025503.1; ENSSBOG00000029207.1.
DR GeneID; 101050442; -.
DR KEGG; sbq:101050442; -.
DR CTD; 56950; -.
DR GeneTree; ENSGT00940000157082; -.
DR OMA; QNWHPSE; -.
DR OrthoDB; 166337at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046975; F:histone H3K36 methyltransferase activity; IEA:Ensembl.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR CDD; cd19202; SET_SMYD2; 1.
DR Gene3D; 1.10.220.160; -; 1.
DR Gene3D; 1.25.40.970; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044419; SMYD2_SET.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR12197; HISTONE-LYSINE N-METHYLTRANSFERASE SMYD; 1.
DR PANTHER; PTHR12197:SF193; N-LYSINE METHYLTRANSFERASE SMYD2; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 7..241
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 52..90
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
SQ SEQUENCE 433 AA; 49748 MW; 3D2E9B3A6255A8ED CRC64;
MWAEGLGGLE RFCSPGKGRG LRALEPFQVG DLLFSCPAYA YVLTVNERGN HCEYCFARKE
GLSKCGRCKQ AFYCNVECQK EDWPMHKLEC SPMVVFGENW NPSETVRLTA RILAKQKIHP
ERTPSERLLA VKEFESHLDK LDNEKKDLIQ SDIAALHHFY SKHLEFPDND SLVVLFAQVN
CNGFTIEDEE LSHLGSAIFP DVALMNHSCC PNVIVTYKGT LAEVRAVQEI SPGEEVFTSY
IDLLYPTEDR NDRLRDSYFF TCECQECTTK DKDKAKVEIR KLSDPPKAEA IRDMVRYARN
VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC LYMQDWEGAL
QYGQKIIKPY SKHYPLYSLN VASMWLKLGR LYMGLEHKAA GEKALKKAIA IMEVAHGKDH
PYISEIKQEI ESH
//
